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Literature summary for 1.16.3.1 extracted from

  • Lovstad, R.A.
    A kinetic study on the phenothiazine dependent oxidation of NADH by bovine ceruloplasmin (2006), Biometals, 19, 1-5.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
chlorpromazine formation of a complex with ceroluplasmin and stimulation. Good correlation of stability of enzyme-drug complex and electron donor ability of the drug molecule Bos taurus
levopromazine formation of a complex with ceroluplasmin and stimulation. Good correlation of stability of enzyme-drug complex and electron donor ability of the drug molecule Bos taurus
promazine formation of a complex with ceroluplasmin and stimulation. Good correlation of stability of enzyme-drug complex and electron donor ability of the drug molecule Bos taurus
triflupromazine formation of a complex with ceroluplasmin and stimulation. Good correlation of stability of enzyme-drug complex and electron donor ability of the drug molecule Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.14
-
NADH pH 6.0, 30°C, presence of triflupromazine Bos taurus
0.21
-
NADH pH 6.0, 30°C, presence of levomepromazine Bos taurus
0.22
-
NADH pH 6.0, 30°C, presence of chlorpromazine Bos taurus
0.23
-
NADH pH 6.0, 30°C, presence of promazine Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + O2
-
Bos taurus NAD+ + H2O
-
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